Origin of the bimodal ?melting? endotherm of ?-form crystallites in wool keratin

Author(s):  
Jinan Cao
Nanomaterials ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 1068
Author(s):  
Xinyue Zhang ◽  
Yani Guo ◽  
Wenjun Li ◽  
Jinyuan Zhang ◽  
Hailiang Wu ◽  
...  

The treatment of wastewater containing heavy metals and the utilization of wool waste are very important for the sustainable development of textile mills. In this study, the wool keratin modified magnetite (Fe3O4) powders were fabricated by using wool waste via a co-precipitation technique for removal of Cu2+ ions from aqueous solutions. The morphology, chemical compositions, crystal structure, microstructure, magnetism properties, organic content, and specific surface area of as-fabricated powders were systematically characterized by various techniques including field emission scanning electron microscopy (FESEM), energy dispersive spectroscopy (EDS), X-ray diffraction (XRD), transmission electron microscopy (TEM), X-ray photoelectron spectroscopy (XPS), vibrating sample magnetometer (VSM), thermogravimetric (TG) analysis, and Brunauer–Emmett–Teller (BET) surface area analyzer. The effects of experimental parameters such as the volume of wool keratin hydrolysate, the dosage of powder, the initial Cu2+ ion concentration, and the pH value of solution on the adsorption capacity of Cu2+ ions by the powders were examined. The experimental results indicated that the Cu2+ ion adsorption performance of the wool keratin modified Fe3O4 powders exhibited much better than that of the chitosan modified ones with a maximum Cu2+ adsorption capacity of 27.4 mg/g under favorable conditions (0.05 g powders; 50 mL of 40 mg/L CuSO4; pH 5; temperature 293 K). The high adsorption capacity towards Cu2+ ions on the wool keratin modified Fe3O4 powders was primarily because of the strong surface complexation of –COOH and –NH2 functional groups of wool keratins with Cu2+ ions. The Cu2+ ion adsorption process on the wool keratin modified Fe3O4 powders followed the Temkin adsorption isotherm model and the intraparticle diffusion and pseudo-second-order adsorption kinetic models. After Cu2+ ion removal, the wool keratin modified Fe3O4 powders were easily separated using a magnet from aqueous solution and efficiently regenerated using 0.5 M ethylene diamine tetraacetic acid (EDTA)-H2SO4 eluting. The wool keratin modified Fe3O4 powders possessed good regenerative performance after five cycles. This study provided a feasible way to utilize waste wool textiles for preparing magnetic biomass-based adsorbents for the removal of heavy metal ions from aqueous solutions.


2005 ◽  
Vol 7 (8) ◽  
pp. 606 ◽  
Author(s):  
Haibo Xie ◽  
Shenghai Li ◽  
Suobo Zhang

1996 ◽  
Vol 462 ◽  
Author(s):  
R. Srjnivasan ◽  
K. A. Jakes

ABSTRACTThe research reported herein is directed toward the determination of the microstructure of silk fibers recovered from the shipwreck site of the S.S. Central America. The structural data obtained from examination of these silk materials using SEM, EDS, and DSC was compared to data obtained from the examination of historic silk fibers (ca. 1860–1880) not exposed to the deep-ocean and of modern silk fibers. Marine silks appear more degraded than historic and modern silk when viewed under the SEM and the fiber surfaces are partially obscured by inorganic deposits. The melting endotherm of marine, historic, and modern silk fibers are comparable to each other, but the glass transition observed in the modern silk is not apparent in the DSC trace of any of the marine silks.


2009 ◽  
Vol 2009 ◽  
pp. 1-5 ◽  
Author(s):  
Jeanette M. Cardamone ◽  
Alberto Nuñez ◽  
Rafael A. Garcia ◽  
Mila Aldema-Ramos

Keratin from wool is a reactive, biocompatible, and biodegradable material. As the biological structural component of skin (soft keratins) and of nails, claws, hair, horn, feathers, and scales (hard keratins) pure keratin comprises up to 90% by weight of wool. Wool was treated in alkaline solutions to extract from 68% to 82% keratin within 2 to 5 hours of exposure at . The keratin products were water-soluble and were confirmed to contain intermediate filament and microfibrillar component-proteins of fractured, residual cuticle, and cortical cells. Oxidation of wool by peroxycarboximidic acid in alkaline hydrogen peroxide produced keratin products with distinct microcrystalline structures: descaled fibers, fibrous matrices, and lyophilized powders. Morphology and confirmation of peptide functionality were documented by SEM, Amino Acid Analysis, SDS-PAGE gel electrophoresis, MALDI-TOF/TOF, and FTIR analyses. The reactivity of keratin from wool models the reactivity of keratin from low-value sources such as cattle hair.


1951 ◽  
Vol 7 ◽  
pp. 547-562 ◽  
Author(s):  
W.R. Middlebrook
Keyword(s):  

1967 ◽  
Vol 120 (2) ◽  
pp. 249-254 ◽  
Author(s):  
R. DeDeurwaerder ◽  
M.G. Dobb ◽  
L.A. Holt ◽  
S.J. Leach

2009 ◽  
Vol 34 (3) ◽  
pp. 399-402 ◽  
Author(s):  
Ryota Hatakeyama ◽  
Yuki Tomita ◽  
Shoji Takigami

1950 ◽  
Vol 47 (4) ◽  
pp. 443-451 ◽  
Author(s):  
S. Blackburn
Keyword(s):  

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